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Mol Cell Biol, March 1998, p. 1266-1274, Vol. 18, No. 3
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Functional Interference of Sp1 and NF-kappa B through the Same DNA Binding Site

Fuminori Hirano,1 Hirotoshi Tanaka,2 Yoshiko Hirano,1 Masaki Hiramoto,3 Hiroshi Handa,3 Isao Makino,2 and Claus Scheidereit1,*

Max Delbrück Center for Molecular Medicine MDC, 13122 Berlin, Germany,1 and Second Department of Internal Medicine, Asahikawa Medical College, Asahikawa 078,2 and Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama 228,3 Japan

Received 15 October 1997/Accepted 5 December 1997

Gene activation by NF-kappa B/Rel transcription factors is modulated by synergistic or antagonistic interactions with other promoter-bound transcription factors. For example, Sp1 sites are often found in NF-kappa B-regulated genes, and Sp1 can activate certain promoters in synergism with NF-kappa B through nonoverlapping binding sites. Here we report that Sp1 acts directly through a subset of NF-kappa B binding sites. The DNA binding affinity of Sp1 to these NF-kappa B sites, as determined by their relative dissociation constants and their relative efficiencies as competitor DNAs or as binding site probes, is in the order of that for a consensus GC box Sp1 site. In contrast, NF-kappa B does not bind to a GC box Sp1 site. Sp1 can activate transcription through immunoglobulin kappa-chain enhancer or P-selectin promoter NF-kappa B sites. p50 homodimers replace Sp1 from the P-selectin promoter by binding site competition and thereby either inhibit basal Sp1-driven expression or, in concert with Bcl-3, stimulate expression. The interaction of Sp1 with NF-kappa B sites thus provides a means to keep an elevated basal expression of NF-kappa B-dependent genes in the absence of activated nuclear NF-kappa B/Rel.

* Corresponding author. Mailing address: Max Delbrück Center for Molecular Medicine, Robert-Rössle-Str. 10, 13122 Berlin, Germany. Phone: 49-30-9406-3816. Fax: 49-30-9406-3866. E-mail: scheidereit{at}mdc-berlin.de.




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